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A more recent version of this article appeared on February 1, 2006
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Submitted on September 30, 2005
Revised on November 4, 2005
Accepted on November 17, 2005
*Laboratoire de Biologie Moléculaire Eucaryote du CNRS, UMR5099, IFR109, 31062 Toulouse, France; Institut de Génétique Moléculaire, 34000 Montpellier, France; Biological Research Center, Hungarian Academy of Sciences, H-6701 Szeged, Hungary
Monitoring Editor: Marvin P. Wickens
Telomerase is a ribonucleoprotein enzyme that counteracts replicative telomere erosion by adding telomeric sequence repeats onto chromosome ends. Despite its well established role in telomere synthesis, telomerase has not yet been detected at telomeres. The RNA component of human telomerase (hTR) resides in the nucleoplasmic Cajal bodies (CBs) of interphase cancer cells. Here, in situ hybridization demonstrates that in human HeLa and Hep2 S phase cells, besides accumulating in CBs, hTR specifically concentrates at a few telomeres which also accumulate the TRF1 and TRF2 telomere marker proteins. Surprisingly, telomeres accumulating hTR exhibit a great accessibility for in situ oligonucleotide hybridization without chromatin denaturation, suggesting that they represent a structurally distinct, minor subset of HeLa telomeres. Moreover, we demonstrate that more than 25% of telomeres accumulating hTR colocalize with CBs. Time-lapse fluorescence microscopy demonstrates that CBs moving in the nucleoplasm of S phase cells transiently associate for 10-40 min with telomeres. Our data raise the intriguing possibility that CBs may deliver hTR to telomeres and/or may function in other aspects of telomere maintenance.
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